GUAA_EHRRG
ID GUAA_EHRRG Reviewed; 528 AA.
AC Q5FF75;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=GMP synthase [glutamine-hydrolyzing] {ECO:0000255|HAMAP-Rule:MF_00344};
DE EC=6.3.5.2 {ECO:0000255|HAMAP-Rule:MF_00344};
DE AltName: Full=GMP synthetase {ECO:0000255|HAMAP-Rule:MF_00344};
DE AltName: Full=Glutamine amidotransferase {ECO:0000255|HAMAP-Rule:MF_00344};
GN Name=guaA {ECO:0000255|HAMAP-Rule:MF_00344};
GN OrderedLocusNames=ERGA_CDS_00650;
OS Ehrlichia ruminantium (strain Gardel).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=302409;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gardel;
RX PubMed=16547041; DOI=10.1128/jb.188.7.2533-2542.2006;
RA Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y.,
RA Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.;
RT "Comparative genomic analysis of three strains of Ehrlichia ruminantium
RT reveals an active process of genome size plasticity.";
RL J. Bacteriol. 188:2533-2542(2006).
CC -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000255|HAMAP-
CC Rule:MF_00344}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2
CC H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00344};
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00344}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00344}.
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DR EMBL; CR925677; CAI27517.1; -; Genomic_DNA.
DR RefSeq; WP_011255266.1; NC_006831.1.
DR AlphaFoldDB; Q5FF75; -.
DR SMR; Q5FF75; -.
DR EnsemblBacteria; CAI27517; CAI27517; ERGA_CDS_00650.
DR KEGG; erg:ERGA_CDS_00650; -.
DR HOGENOM; CLU_014340_0_5_5; -.
DR OMA; KRKIIGH; -.
DR OrthoDB; 504464at2; -.
DR BioCyc; ERUM302409:ERGA_RS00340-MON; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000000533; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01742; GATase1_GMP_Synthase; 1.
DR CDD; cd01997; GMP_synthase_C; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_00344; GMP_synthase; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR001674; GMP_synth_C.
DR InterPro; IPR004739; GMP_synth_GATase.
DR InterPro; IPR022955; GMP_synthase.
DR InterPro; IPR025777; GMPS_ATP_PPase_dom.
DR InterPro; IPR022310; NAD/GMP_synthase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF00958; GMP_synt_C; 1.
DR Pfam; PF02540; NAD_synthase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR00884; guaA_Cterm; 1.
DR TIGRFAMs; TIGR00888; guaA_Nterm; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glutamine amidotransferase; GMP biosynthesis; Ligase;
KW Nucleotide-binding; Purine biosynthesis.
FT CHAIN 1..528
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_0000229426"
FT DOMAIN 3..199
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT DOMAIN 200..394
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 83
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 174
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 176
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT BINDING 227..233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
SQ SEQUENCE 528 AA; 59204 MW; 914777CBB96E1A25 CRC64;
MSKVAIIDFG SQFTQLLARR IRDLNIYSEI FLPNVAFDLI KGVDAFILSG GPRSVPNSDG
IPKIVHDILQ FNEKTSIPVL GICYGLQILS NYFESDVVSN CNKEFGKTIL NIIKNSKIIE
NIWESGDQAY VWMSHADSVY NIPRGFEVIA YSVLNNSIAM VANEQRRIYG MQFHPEVYHT
PDGINLLANF LDIAGCQKDW TVTSFIDDQQ DAIKKQIGNK KVIAALSGGV DSSVAAALTY
KAIGDQLHCV FIDNGLLRYN EVEKVKQLFI NELKIPVTIV DKSAVFLNRL KSITDPERKR
KIIGETFIEI FEEEANKLEG VEFLMQGTIY PDVVESGGSG SIAKESVVIK SHHNVGGLPK
TMKFKLVEPL KYLFKDEVRI LGRNLGISTE ILMRHPFPGP GLAVRIIGEI TEEKVKMLQA
ADDIYINLIK KYELYDVMWQ AFVVLLPVKT VGVMGDRRTY GHACVLRAVN SHDGMTAESF
PFCMDEETQW KFFKCIQEAS NAIINSVNGI NRVAYDITSK PPATIEWE
